The CHST family is comprised of 14 enzymes in human. All members of this family are Golgi-localized type II membrane proteins (1). Only the luminal and enzymatic domain is expressed in each of our recombinant CHST proteins. These enzymes transfer sulfate (i.e., sulfonate) onto the 6 O or 4O positions of GalNAc, Gal and GlcNAc residues on glycoproteins, proteoglycans and glycolipids (2). This sulfation often creates specific epitopes that can be recognized by extracellular matrix proteins, cell surface receptors and viruses (3). CHST4, also known as high endothelial cells Nacetylglucosamine 6Osulfotransferase (HECGlcNAc6ST) or L-selectin ligand sulfotransferases (LSST), catalyzes the transfer of sulfate to position 6 of non reducing GlcNAc residues within mucin-associated glycans that ultimately serve as L selectin ligands (4). It has a catalytic preference for core 2-branched mucin-type O glycans, but also has activity toward core 3 type of O glycan 5). Human CHST4 shares 72% amino acid sequence identity with the mouse ortholog. Chinese Hamster Ovary cell line, CHO-derived mouse Carbohydrate Sulfotransferase 4/CHST4 protein, Arg30-Gly388 with an N-terminal 6-His tag. Accession Q9R1I1 Activity: Measured by its ability to transfer sulfate from PAPS to N-acetyl-D-glucosamine. The specific activity is >35 pmol/min/ug, measured under the described conditions. Applications: Suitable for use in ELISA. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: 12 months from date of receipt, 20 to 70C as supplied. 1 month, 2 to 8C under sterile conditions after reconstitution. months, 20 to 70C under sterile conditions after reconstitution. Avoid repeated freeze thaw cycles.
